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Published online
doi:10.1083/jcb.200805147
The Journal of Cell Biology, Vol. 184, No. 2, 253-267
The Rockefeller University Press, 0021-9525 $30.00
© Chandra Roy et al.
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Article

Kank attenuates actin remodeling by preventing interaction between IRSp53 and Rac1



Badal Chandra Roy, Naoto Kakinuma, and Ryoiti Kiyama

Neuroscience Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan

Correspondence to Ryoiti Kiyama: kiyama.r{at}aist.go.jp

In this study, insulin receptor substrate (IRS) p53 is identified as a binding partner for Kank, a kidney ankyrin repeat–containing protein that functions to suppress cell proliferation and regulate the actin cytoskeleton. Kank specifically inhibits the binding of IRSp53 with active Rac1 (Rac1G12V) but not Cdc42 (cdc42G12V) and thus inhibits the IRSp53-dependent development of lamellipodia without affecting the formation of filopodia. Knockdown (KD) of Kank by RNA interference results in increased lamellipodial development, whereas KD of both Kank and IRSp53 has little effect. Moreover, insulin-induced membrane ruffling is inhibited by overexpression of Kank. Kank also suppresses integrin-dependent cell spreading and IRSp53-induced neurite outgrowth. Our results demonstrate that Kank negatively regulates the formation of lamellipodia by inhibiting the interaction between Rac1 and IRSp53.

B.C. Roy and N. Kakinuma contributed equally to this paper.

Abbreviations used in this paper: CRIB, cdc42/Rac1 interactive binding; esiRNA, endoribonuclease-prepared siRNA; F-actin, filamentous actin; IRS, insulin receptor substrate; KD, knockdown; MBP, maltose-binding protein; mIRS, mouse IRSp53; WASP, Wiskott-Aldrich syndrome protein.

© 2009 Roy et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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